Litcius/Paper detail

Inhibition of Human Salivary and Pancreatic α-Amylase by Resveratrol Oligomers

Rizliya Visvanathan, Dang Truong Le, Sushil Dhital, Topul Rali, Rohan A. Davis, Gary Williamson

2024Journal of Medicinal Chemistry11 citationsDOIOpen Access PDF

Abstract

High Resolution Image Download MS PowerPoint Slide A key strategy to mitigate postprandial hyperglycemia involves inhibiting α-amylases, which commence the starch digestion process in the gut. This study examined the inhibitory effects of resveratrol and stilbenoid tetramers, vaticanol B, (−)-hopeaphenol, and vatalbinoside A on human salivary and pancreatic α-amylases experimentally and through molecular docking studies. Vaticanol B demonstrated the most potent inhibition with IC 50 values of 5.3 ± 0.3 μM for salivary and 6.1 ± 0.5 μM for pancreatic α-amylase (compared to acarbose with IC 50 values of 1.2 ± 0.1 μM and 0.5 ± 0.0 μM, respectively). Kinetic analysis suggested a competitive inhibition mode for vaticanol B. Resveratrol and vatalbinoside A were poor inhibitors of human α-amylases, while (−)-hopeaphenol exhibited moderate inhibition. Molecular docking supported the inhibition data, and several aspects of the structural configurations explained the stronger inhibition exerted by vaticanol B. Overall, vaticanol B shows promise as a natural alternative to acarbose for inhibiting α-amylase.

Topics & Concepts

ChemistryAmylaseResveratrolBiochemistrySalivaEnzymeSirtuins and Resveratrol in MedicinePancreatic function and diabetesBiochemical effects in animals
Inhibition of Human Salivary and Pancreatic α-Amylase by Resveratrol Oligomers | Litcius